1ma9
From Proteopedia
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| - | [[Image:1ma9.jpg|left|200px]] | + | [[Image:1ma9.jpg|left|200px]] |
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| - | '''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin''' | + | {{Structure |
| + | |PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MA9 is a [ | + | 1MA9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MA9 OCA]. |
==Reference== | ==Reference== | ||
| - | Actin-DBP: the perfect structural fit?, Verboven C, Bogaerts I, Waelkens E, Rabijns A, Van Baelen H, Bouillon R, De Ranter C, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):263-73. Epub 2003, Jan 23. PMID:[http:// | + | Actin-DBP: the perfect structural fit?, Verboven C, Bogaerts I, Waelkens E, Rabijns A, Van Baelen H, Bouillon R, De Ranter C, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):263-73. Epub 2003, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554937 12554937] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:58 2008'' |
Revision as of 10:40, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin
Contents |
Overview
The multifunctional vitamin D binding protein (DBP) is an actin-sequestering protein present in blood. The crystal structure of the actin-DBP complex was determined at 2.4 A resolution. DBP binds to actin subdomains 1 and 3 and occludes the cleft at the interface between these subdomains. Most remarkably, DBP demonstrates an unusually large actin-binding interface, far exceeding the binding-interface areas reported for other actin-binding proteins such as profilin, DNase I and gelsolin. The fast-growing side of actin monomers is blocked completely through a perfect structural fit with DBP, demonstrating how DBP effectively interferes with actin-filament formation. It establishes DBP as the hitherto best actin-sequestering protein and highlights its key role in suppressing and preventing extracellular actin polymerization.
Disease
Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[139200]
About this Structure
1MA9 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Actin-DBP: the perfect structural fit?, Verboven C, Bogaerts I, Waelkens E, Rabijns A, Van Baelen H, Bouillon R, De Ranter C, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):263-73. Epub 2003, Jan 23. PMID:12554937
Page seeded by OCA on Thu Mar 20 12:40:58 2008
